Type II Cadherin Ectodomain Structures: Implications for Classical Cadherin Specificity

Journal Article · Sun Jan 01 04:00:00 EST 2006 · Cell

DOI:https://doi.org/10.1016/j.cell.2005.12.046· OSTI ID:914088

Patel, S; Ciatto, C; Chen, C; Bahna, F; Rajebhosale, M; Arkus, N; Schieren, I; Jessell, T; Honig, B

Type I and II classical cadherins help to determine the adhesive specificities of animal cells. Crystal-structure determination of ectodomain regions from three type II cadherins reveals adhesive dimers formed by exchange of N-terminal {beta} strands between partner extracellular cadherin-1 (EC1) domains. These interfaces have two conserved tryptophan side chains that anchor each swapped strand, compared with one in type I cadherins, and include large hydrophobic regions unique to type II interfaces. The EC1 domains of type I and type II cadherins appear to encode cell adhesive specificity in vitro. Moreover, perturbation of motor neuron segregation with chimeric cadherins depends on EC1 domain identity, suggesting that this region, which includes the structurally defined adhesive interface, encodes type II cadherin functional specificity in vivo.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 914088
• Report Number(s): BNL--78656-2007-JA
• Journal Information: Cell, Journal Name: Cell Journal Issue: 6 Vol. 124; ISSN 0092-8674; ISSN CELLB5
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
43 PARTICLE ACCELERATORS
ADHESIVES
ANIMAL CELLS
CHAINS
CRYSTAL STRUCTURE
DIMERS
FUNCTIONALS
IN VITRO
IN VIVO
NERVE CELLS
NSLS
SEGREGATION
SPECIFICITY
TRYPTOPHAN
national synchrotron light source